Research at Yale

From WikidChem

Beta(3)-peptides are polymeric molecules composed of Beta(3)-amino acids. They adopt a discrete three-dimensional conformation dictated by their primary sequence and facilitated by noncovalent interactions. Polymers that display such folding characteristics fall under the category of “foldamers.” Research on these peptides has burgeoned in recent years. While maintaining the possibility of acting as pseudo-proteins by bearing proteinogenic side-chains, Beta(3)-peptides also have the potential of exceeding natural proteins in their use in medicinal and therapeutic applications, because they are not susceptible to degradation by proteases. Beta(3)-peptide research started with the synthesis of simple trimeric peptides. These short fragments were too unstructured to yield insight into the possibility of higher ordered Beta(3)-peptide structure, but subsequent research on longer peptides showed that it was possible to form helices, turns and sheets. The current frontier of Beta(3)-peptide research lies in developing the three-dimensional conformation of these peptides past secondary structure and into controlled tertiary and quaternary structure. Only by achieving control of higher-ordered structure can true function be engineered into this promising class of molecules.

In the Schepartz lab, we have focused on developing oligomeric helical bundles of Beta(3)-peptides. Much insight has been gained into the forces that drive their oligomerization as well as their similarities to natural proteins and peptides.

For a list of our publications, please follow this link.